[Count Henri de Bonneval (1806-1882), practitioner of homeopathy, agronomist and philanthropist].

Count Henri de Bonneval, was born in Bordeaux in 1806, in the line of descent of one of the most ancient French families of noble rank. He was assistant manager of the Strasbourg stud farm in 1830, when Louis-Philippe, an Orleanist, ascended to the throne of the Bourbon Charles X. As several other legitimists, Count Henri refused to take an oath to the new king and prefered to resign his position.

[Jean Guillaume Auguste Lugol (1788-1851): his life and his works: a brief encounter, 150 years after his death].

J.G.A.

Biochemical basis of the pharmacologic action of chondroitin sulfates on the osteoarticular system.

Background: Chondroitin sulfates (CS) are involved in articular metabolism and could be used as therapeutic agents in degenerative articular diseases.

Objectives: To review the published reports describing both the metabolism of glycosaminoglycans (GAG) and their involvement in osteoarticular pathophysiology.

Methods: MEDLINE search for relevant articles and review of cited references.

Calcium and bicarbonate ions mediate the inhibition of mast cell histamine release by Avène spa water.

Avène spa water (ASW) inhibits the histamine release induced in mast cells by substance P; the inhibition is reversed by EDTA and by EGTA. Calcium and magnesium ions, the major cations present in ASW, were experimented in simple saline solutions in the presence of various counter-ions. Only calcium salts inhibited the peptidergic stimulation, with different potencies ruled by the nature of the counter-anion (HCO3- > Cl- > SO4(2)).

Effect of the phosphonic analogue of tyrosine on tyrosine iodination.

Depositing ofDL-1-amino-2-(p-hydroxyphenyl)-ethylphosphonic acid (Tyr-P) on the chicken embryo induced a dose dependent decrease of the iodine uptake by the embryonic thyroid. Tyr-P interfered on iodination of tyrosine when tested with hog thyroid peroxidase (TPO) and with bovine lactoperoxidase (LPO); the analogue was recognized by the two enzymes but its affinity for TPO and LPO was respectively 3 and 7 fold higher compared with that of the natural substrate, suggesting that Tyr-P may act as an iodine trap.